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Protein

Probable low-specificity L-threonine aldolase 2

Gene

THA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Threonine aldolase involved in threonine degradation to glycine. May play a role in the removal of L-allo-threonine.1 Publication

Catalytic activityi

L-threonine = glycine + acetaldehyde.
L-allo-threonine = glycine + acetaldehyde.

Cofactori

Kineticsi

  1. KM=3.8 mM for L-threonine1 Publication

Pathwayi

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. threonine aldolase activity Source: TAIR

GO - Biological processi

  1. threonine catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:GQT-2165-MONOMER.
BRENDAi2.1.2.1. 302.
UniPathwayiUPA00044; UER00429.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable low-specificity L-threonine aldolase 2 (EC:4.1.2.48)
Alternative name(s):
Threonine aldolase 2
Gene namesi
Name:THA2
Ordered Locus Names:At3g04520
ORF Names:T27C4.17
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G04520.

Pathology & Biotechi

Disruption phenotypei

Lethal albino phenotype when homozygous.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355Probable low-specificity L-threonine aldolase 2PRO_0000428660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei211 – 2111N6-(pyridoxal phosphate)lysineBy similarity

Expressioni

Tissue specificityi

Expressed in roots, leaf vasculature and flowers.1 Publication

Gene expression databases

ExpressionAtlasiQ9FPH3. baseline and differential.
GenevestigatoriQ9FPH3.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G04520.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9FPH3.
SMRiQ9FPH3. Positions 10-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the threonine aldolase family.Curated

Phylogenomic databases

eggNOGiCOG2008.
InParanoidiQ9FPH3.
KOiK01620.
OMAiEVGDEQI.
PhylomeDBiQ9FPH3.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FPH3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVTPTTIRTV DLRSDTVTKP TESMRSAMAN AEVDDDVLGN DPTALRLEKE
60 70 80 90 100
VAEIAGKEAA MFVPSGTMGN LISVLVHCDE RGSEVILGDD SHIHIYENGG
110 120 130 140 150
VSSLGGVHPR TVKNEEDGTM EIGAIEAAVR SPKGDLHHPV TKLICLENTQ
160 170 180 190 200
ANCGGRCLPI EYIDKVGELA KKHGLKLHID GARIFNASVA LGVPVKRIVQ
210 220 230 240 250
AADSVSICLS KGIGAPVGSV IVGSKKFITK ARWLRKTLGG GMRQIGVLCA
260 270 280 290 300
AALVALHENV AKLEDDHKKA RVLAEGLNRI ERLRVNVAAV ETNIIYVDIP
310 320 330 340 350
EDPKFGAEEA CKSLEDVGVL VIPQATFRIR IVLHHQISDV DVEYVLSCFE

KIFHS
Length:355
Mass (Da):38,252
Last modified:March 1, 2001 - v1
Checksum:iD7D1EFDBA18B517E
GO

Sequence cautioni

The sequence AAF63783.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC022287 Genomic DNA. Translation: AAF63783.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74091.1.
AF325033 mRNA. Translation: AAG40385.1.
AY091093 mRNA. Translation: AAM14044.1.
AY123033 mRNA. Translation: AAM67566.1.
AK175345 mRNA. Translation: BAD43108.1.
AY085456 mRNA. Translation: AAM62682.1.
RefSeqiNP_566228.1. NM_111323.3. [Q9FPH3-1]
UniGeneiAt.19145.

Genome annotation databases

EnsemblPlantsiAT3G04520.1; AT3G04520.1; AT3G04520. [Q9FPH3-1]
GeneIDi819608.
KEGGiath:AT3G04520.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC022287 Genomic DNA. Translation: AAF63783.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE74091.1.
AF325033 mRNA. Translation: AAG40385.1.
AY091093 mRNA. Translation: AAM14044.1.
AY123033 mRNA. Translation: AAM67566.1.
AK175345 mRNA. Translation: BAD43108.1.
AY085456 mRNA. Translation: AAM62682.1.
RefSeqiNP_566228.1. NM_111323.3. [Q9FPH3-1]
UniGeneiAt.19145.

3D structure databases

ProteinModelPortaliQ9FPH3.
SMRiQ9FPH3. Positions 10-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G04520.1-P.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G04520.1; AT3G04520.1; AT3G04520. [Q9FPH3-1]
GeneIDi819608.
KEGGiath:AT3G04520.

Organism-specific databases

TAIRiAT3G04520.

Phylogenomic databases

eggNOGiCOG2008.
InParanoidiQ9FPH3.
KOiK01620.
OMAiEVGDEQI.
PhylomeDBiQ9FPH3.

Enzyme and pathway databases

UniPathwayiUPA00044; UER00429.
BioCyciARA:GQT-2165-MONOMER.
BRENDAi2.1.2.1. 302.

Gene expression databases

ExpressionAtlasiQ9FPH3. baseline and differential.
GenevestigatoriQ9FPH3.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR001597. ArAA_b-elim_lyase/Thr_aldolase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR023603. Threonine_aldolase.
[Graphical view]
PfamiPF01212. Beta_elim_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017617. Thr_aldolase. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Two Arabidopsis threonine aldolases are nonredundant and compete with threonine deaminase for a common substrate pool."
    Joshi V., Laubengayer K.M., Schauer N., Fernie A.R., Jander G.
    Plant Cell 18:3564-3575(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Entry informationi

Entry nameiTHA2_ARATH
AccessioniPrimary (citable) accession number: Q9FPH3
Secondary accession number(s): Q9M835
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.